Kataoka M, Nakamura Y, Urano N, Ishige T, Shi G, Kita S, Sakamoto K, Shimizu S
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Lett Appl Microbiol. 2006 Oct;43(4):430-5. doi: 10.1111/j.1472-765X.2006.01970.x.
A novel NADP(+)-dependent L-1-amino-2-propanol dehydrogenase was isolated from Rhodococcus erythropolis MAK154, and characterized.
The enzyme was inducibly produced on cultivation with aminoalcohols such as 1-amino-2-propanol, 1-amino-2-butanol and 2-aminocyclohexanol. The enzyme catalyses the NADP(+)-dependent oxidation of several aminoalcohols, and also the NADPH-dependent asymmetric reduction of an aminoketone compound to a double chiral aminoalcohol, d-pseudoephedrine. Amino acid sequence analysis showed that the enzyme might belong to the short-chain dehydrogenase/reductase family.
NADP(+)-dependent L-1-amino-2-propanol dehydrogenase isolated from R. erythropolis MAK154 reversibly catalysed dehydrogenation of aminoalcohols, and exhibited a unique sterospecifity for the reduction reaction.
The enzyme is a promising catalyst for the production of double chiral compound, d-pseudoephedrine, from prochiral substrate.
从红平红球菌MAK154中分离并鉴定一种新型的依赖烟酰胺腺嘌呤二核苷酸磷酸（NADP(+)）的L-1-氨基-2-丙醇脱氢酶。
该酶在用氨基醇（如1-氨基-2-丙醇、1-氨基-2-丁醇和2-氨基环己醇）培养时可诱导产生。该酶催化多种氨基醇的NADP(+)依赖性氧化反应，还催化氨基酮化合物的NADPH依赖性不对称还原反应生成双手性氨基醇d-伪麻黄碱。氨基酸序列分析表明该酶可能属于短链脱氢酶/还原酶家族。
从红平红球菌MAK154中分离得到的依赖NADP(+)的L-1-氨基-2-丙醇脱氢酶可逆地催化氨基醇的脱氢反应，并且在还原反应中表现出独特的立体特异性。
该酶是一种有前景的催化剂，可用于从前手性底物生产双手性化合物d-伪麻黄碱。
